ID   CLPX_RICPU              Reviewed;         425 AA.
AC   C4K2L5;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   07-JUL-2009, sequence version 1.
DT   03-AUG-2022, entry version 69.
DE   RecName: Full=ATP-dependent Clp protease ATP-binding subunit ClpX {ECO:0000255|HAMAP-Rule:MF_00175};
GN   Name=clpX {ECO:0000255|HAMAP-Rule:MF_00175}; OrderedLocusNames=RPR_06610;
OS   Rickettsia peacockii (strain Rustic).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC   Rickettsiaceae; Rickettsieae; Rickettsia; spotted fever group.
OX   NCBI_TaxID=562019;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Rustic;
RX   PubMed=20027221; DOI=10.1371/journal.pone.0008361;
RA   Felsheim R.F., Kurtti T.J., Munderloh U.G.;
RT   "Genome sequence of the endosymbiont Rickettsia peacockii and comparison
RT   with virulent Rickettsia rickettsii: identification of virulence factors.";
RL   PLoS ONE 4:E8361-E8361(2009).
CC   -!- FUNCTION: ATP-dependent specificity component of the Clp protease. It
CC       directs the protease to specific substrates. Can perform chaperone
CC       functions in the absence of ClpP. {ECO:0000255|HAMAP-Rule:MF_00175}.
CC   -!- SUBUNIT: Component of the ClpX-ClpP complex. Forms a hexameric ring
CC       that, in the presence of ATP, binds to fourteen ClpP subunits assembled
CC       into a disk-like structure with a central cavity, resembling the
CC       structure of eukaryotic proteasomes. {ECO:0000255|HAMAP-Rule:MF_00175}.
CC   -!- SIMILARITY: Belongs to the ClpX chaperone family. {ECO:0000255|HAMAP-
CC       Rule:MF_00175}.
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DR   EMBL; CP001227; ACR47812.1; -; Genomic_DNA.
DR   AlphaFoldDB; C4K2L5; -.
DR   SMR; C4K2L5; -.
DR   EnsemblBacteria; ACR47812; ACR47812; RPR_06610.
DR   KEGG; rpk:RPR_06610; -.
DR   HOGENOM; CLU_014218_8_2_5; -.
DR   OMA; HYKRVQA; -.
DR   Proteomes; UP000005015; Chromosome.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR   GO; GO:0140662; F:ATP-dependent protein folding chaperone; IEA:InterPro.
DR   GO; GO:0046983; F:protein dimerization activity; IEA:InterPro.
DR   GO; GO:0051082; F:unfolded protein binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   Gene3D; 3.40.50.300; -; 1.
DR   Gene3D; 6.20.220.10; -; 1.
DR   HAMAP; MF_00175; ClpX; 1.
DR   InterPro; IPR003593; AAA+_ATPase.
DR   InterPro; IPR003959; ATPase_AAA_core.
DR   InterPro; IPR019489; Clp_ATPase_C.
DR   InterPro; IPR004487; Clp_protease_ATP-bd_su_ClpX.
DR   InterPro; IPR046425; ClpX_bact.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR010603; Znf_CppX_C4.
DR   InterPro; IPR038366; Znf_CppX_C4_sf.
DR   Pfam; PF07724; AAA_2; 1.
DR   Pfam; PF10431; ClpB_D2-small; 1.
DR   Pfam; PF06689; zf-C4_ClpX; 1.
DR   SMART; SM00382; AAA; 1.
DR   SMART; SM01086; ClpB_D2-small; 1.
DR   SMART; SM00994; zf-C4_ClpX; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   TIGRFAMs; TIGR00382; clpX; 1.
DR   PROSITE; PS51902; CLPX_ZB; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Chaperone; Metal-binding; Nucleotide-binding; Zinc.
FT   CHAIN           1..425
FT                   /note="ATP-dependent Clp protease ATP-binding subunit ClpX"
FT                   /id="PRO_1000203742"
FT   DOMAIN          1..53
FT                   /note="ClpX-type ZB"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01250"
FT   BINDING         12
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01250"
FT   BINDING         15
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01250"
FT   BINDING         34
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01250"
FT   BINDING         37
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01250"
FT   BINDING         117..124
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00175"
SQ   SEQUENCE   425 AA;  46622 MW;  630404DCE50C3B73 CRC64;
     MVVEADKKAL ICSFCSKKQH EVKKLIAGPA VFICDECIDL CTDIMKEENK VALKQITSSI
     PTPQKICGIL NDYVVGQDQA KKILAVAVYN HYKRLEYVQS GNNDVELNKS NILLIGPTGS
     GKTLLAQTLA KILDVPFTMA DATSLTEAGY VGEDVENILL RLLIASEFNI AKAQKGIIYI
     DEVDKIARKS ENPSITRDVS GEGVQQALLK IMEGTVASVP PQGGRKHPQQ DFVQLDTSNI
     LFICGGAFMG IDSIITSRTN HSSIGFAANV NMDKEKNNSE ILKSLEIEDL TKFGLIPEFI
     GRLPIVTTLD ELDKEALITI LTKPKNAIVK QYQKQFELDD AELVIDDSAL ETIAEKALAK
     KTGARGLRSI LEHLLLDSMY KVAELKRQRV TITKEVVNGL VEPIMTSLIS TKSNKKQPII
     ADIPA